DDX20_HUMAN
ID DDX20_HUMAN Reviewed; 824 AA.
AC Q9UHI6; B4DWV7; Q96F72; Q9NVM3; Q9UF59; Q9UIY0; Q9Y659;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX20;
DE EC=3.6.1.15 {ECO:0000269|PubMed:10383418, ECO:0000269|PubMed:20510246};
DE EC=3.6.4.13 {ECO:0000269|PubMed:10383418, ECO:0000269|PubMed:20510246};
DE AltName: Full=Component of gems 3;
DE AltName: Full=DEAD box protein 20;
DE AltName: Full=DEAD box protein DP 103;
DE AltName: Full=Gemin-3;
GN Name=DDX20; Synonyms=DP103, GEMIN3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION IN THE CORE SMN
RP COMPLEX, INTERACTION WITH SNRPB; SNRPD2 AND SNRPD3, SUBCELLULAR LOCATION,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10601333; DOI=10.1083/jcb.147.6.1181;
RA Charroux B., Pellizzoni L., Perkinson R.A., Shevchenko A., Mann M.,
RA Dreyfuss G.;
RT "Gemin3: a novel DEAD box protein that interacts with SMN, the spinal
RT muscular atrophy gene product, and a component of gems.";
RL J. Cell Biol. 147:1181-1194(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH EBV EBNA2 AND EBV
RP EBNA3C, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=10383418; DOI=10.1074/jbc.274.27.19136;
RA Grundhoff A.T., Kremmer E., Tuereci O., Glieden A., Gindorf C., Atz J.,
RA Mueller-Lantzsch N., Schubach W.H., Grasser F.A.;
RT "Characterization of DP103, a novel DEAD box protein that binds to the
RT Epstein-Barr virus nuclear proteins EBNA2 and EBNA3C.";
RL J. Biol. Chem. 274:19136-19144(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Esophagus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-636.
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 189-275 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP INTERACTION WITH SNUPN; SMN1 AND SNRPB, AND SUBCELLULAR LOCATION.
RX PubMed=12095920; DOI=10.1093/hmg/11.15.1785;
RA Narayanan U., Ospina J.K., Frey M.R., Hebert M.D., Matera A.G.;
RT "SMN, the spinal muscular atrophy protein, forms a pre-import snRNP complex
RT with snurportin1 and importin beta.";
RL Hum. Mol. Genet. 11:1785-1795(2002).
RN [8]
RP INTERACTION WITH PPP4R2.
RX PubMed=12668731; DOI=10.1242/jcs.00409;
RA Carnegie G.K., Sleeman J.E., Morrice N., Hastie C.J., Peggie M.W.,
RA Philp A., Lamond A.I., Cohen P.T.W.;
RT "Protein phosphatase 4 interacts with the survival of motor neurons complex
RT and enhances the temporal localisation of snRNPs.";
RL J. Cell Sci. 116:1905-1913(2003).
RN [9]
RP INTERACTION WITH FOXL2.
RX PubMed=16153597; DOI=10.1016/j.bbrc.2005.08.184;
RA Lee K., Pisarska M.D., Ko J.J., Kang Y., Yoon S., Ryou S.M., Cha K.Y.,
RA Bae J.;
RT "Transcriptional factor FOXL2 interacts with DP103 and induces apoptosis.";
RL Biochem. Biophys. Res. Commun. 336:876-881(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-688, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [11]
RP IDENTIFICATION IN THE SMN COMPLEX, AND INTERACTION WITH GEMIN4 AND SMN1.
RX PubMed=17178713; DOI=10.1074/jbc.m608528200;
RA Otter S., Grimmler M., Neuenkirchen N., Chari A., Sickmann A., Fischer U.;
RT "A comprehensive interaction map of the human survival of motor neuron
RT (SMN) complex.";
RL J. Biol. Chem. 282:5825-5833(2007).
RN [12]
RP FUNCTION IN SNRNP BIOGENESIS, AND IDENTIFICATION IN SMN-SM COMPLEX.
RX PubMed=18984161; DOI=10.1016/j.cell.2008.09.020;
RA Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B.,
RA Englbrecht C., Sickmann A., Stark H., Fischer U.;
RT "An assembly chaperone collaborates with the SMN complex to generate
RT spliceosomal SnRNPs.";
RL Cell 135:497-509(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187; THR-552 AND SER-714, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-500; SER-532;
RP THR-552; SER-652; SER-654; SER-656; SER-677; SER-678; SER-703; THR-705 AND
RP SER-714, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677; SER-678 AND SER-703, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672; SER-678 AND SER-714, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP INTERACTION WITH PUM2 AND NANOS1.
RX PubMed=21800163; DOI=10.1007/s00418-011-0842-y;
RA Ginter-Matuszewska B., Kusz K., Spik A., Grzeszkowiak D., Rembiszewska A.,
RA Kupryjanczyk J., Jaruzelska J.;
RT "NANOS1 and PUMILIO2 bind microRNA biogenesis factor GEMIN3, within
RT chromatoid body in human germ cells.";
RL Histochem. Cell Biol. 136:279-287(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505; SER-672; SER-677 AND
RP SER-678, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268; SER-269; SER-505;
RP THR-552; SER-560; SER-672; SER-677; SER-678; SER-703; THR-705 AND SER-714,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [22]
RP INTERACTION WITH GEMIN5.
RX PubMed=33963192; DOI=10.1038/s41467-021-22627-w;
RA Kour S., Rajan D.S., Fortuna T.R., Anderson E.N., Ward C., Lee Y., Lee S.,
RA Shin Y.B., Chae J.H., Choi M., Siquier K., Cantagrel V., Amiel J.,
RA Stolerman E.S., Barnett S.S., Cousin M.A., Castro D., McDonald K.,
RA Kirmse B., Nemeth A.H., Rajasundaram D., Innes A.M., Lynch D., Frosk P.,
RA Collins A., Gibbons M., Yang M., Desguerre I., Boddaert N., Gitiaux C.,
RA Rydning S.L., Selmer K.K., Urreizti R., Garcia-Oguiza A., Osorio A.N.,
RA Verdura E., Pujol A., McCurry H.R., Landers J.E., Agnihotri S.,
RA Andriescu E.C., Moody S.B., Phornphutkul C., Sacoto M.J.G., Begtrup A.,
RA Houlden H., Kirschner J., Schorling D., Rudnik-Schoeneborn S., Strom T.M.,
RA Leiz S., Juliette K., Richardson R., Yang Y., Zhang Y., Wang M., Wang J.,
RA Wang X., Platzer K., Donkervoort S., Boennemann C.G., Wagner M., Issa M.Y.,
RA Elbendary H.M., Stanley V., Maroofian R., Gleeson J.G., Zaki M.S.,
RA Senderek J., Pandey U.B.;
RT "Loss of function mutations in GEMIN5 cause a neurodevelopmental
RT disorder.";
RL Nat. Commun. 12:2558-2558(2021).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 41-268 IN COMPLEX WITH ADP,
RP ADP-BINDING, AND CATALYTIC ACTIVITY.
RX PubMed=20510246; DOI=10.1016/j.jmb.2010.05.046;
RA Schutz P., Wahlberg E., Karlberg T., Hammarstrom M., Collins R., Flores A.,
RA Schuler H.;
RT "Crystal structure of human RNA helicase A (DHX9): structural basis for
RT unselective nucleotide base binding in a DEAD-box variant protein.";
RL J. Mol. Biol. 400:768-782(2010).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 41-268.
RX PubMed=20941364; DOI=10.1371/journal.pone.0012791;
RA Schutz P., Karlberg T., van den Berg S., Collins R., Lehtio L., Hogbom M.,
RA Holmberg-Schiavone L., Tempel W., Park H.W., Hammarstrom M., Moche M.,
RA Thorsell A.G., Schuler H.;
RT "Comparative structural analysis of human DEAD-box RNA helicases.";
RL PLoS ONE 5:E12791-E12791(2010).
CC -!- FUNCTION: The SMN complex catalyzes the assembly of small nuclear
CC ribonucleoproteins (snRNPs), the building blocks of the spliceosome,
CC and thereby plays an important role in the splicing of cellular pre-
CC mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins
CC SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in
CC a heptameric protein ring on the Sm site of the small nuclear RNA to
CC form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1,
CC SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm
CC complex by the chaperone CLNS1A that controls the assembly of the core
CC snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm
CC proteins from CLNS1A forming an intermediate. Binding of snRNA inside
CC 5Sm triggers eviction of the SMN complex, thereby allowing binding of
CC SNRPD3 and SNRPB to complete assembly of the core snRNP. May also play
CC a role in the metabolism of small nucleolar ribonucleoprotein
CC (snoRNPs). {ECO:0000269|PubMed:18984161}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000269|PubMed:10383418, ECO:0000269|PubMed:20510246};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000305|PubMed:10383418};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC Evidence={ECO:0000269|PubMed:10383418, ECO:0000269|PubMed:20510246};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23681;
CC Evidence={ECO:0000305|PubMed:10383418};
CC -!- SUBUNIT: Part of the core SMN complex that contains SMN1, GEMIN2/SIP1,
CC DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP
CC (PubMed:10601333, PubMed:17178713). Part of the SMN-Sm complex that
CC contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6,
CC GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2,
CC SNRPD3, SNRPE, SNRPF and SNRPG (PubMed:18984161, PubMed:12095920).
CC Interacts with SMN1; the interaction is direct (PubMed:17178713).
CC Interacts with GEMIN4; the interaction is direct (PubMed:17178713).
CC Interacts with GEMIN5 (PubMed:33963192). Interacts with SNUPN; the
CC interaction is direct (PubMed:12095920). Interacts with PPP4R2
CC (PubMed:12668731). Interacts with FOXL2 (PubMed:16153597). Interacts
CC with EBV EBNA2 and EBNA3C (PubMed:10383418). Interacts with NANOS1 and
CC PUM2 (PubMed:21800163). {ECO:0000269|PubMed:10383418,
CC ECO:0000269|PubMed:10601333, ECO:0000269|PubMed:12095920,
CC ECO:0000269|PubMed:12668731, ECO:0000269|PubMed:16153597,
CC ECO:0000269|PubMed:17178713, ECO:0000269|PubMed:18984161,
CC ECO:0000269|PubMed:21800163, ECO:0000269|PubMed:33963192}.
CC -!- INTERACTION:
CC Q9UHI6; P01023: A2M; NbExp=3; IntAct=EBI-347658, EBI-640741;
CC Q9UHI6; P50570-2: DNM2; NbExp=3; IntAct=EBI-347658, EBI-10968534;
CC Q9UHI6; Q8TB36: GDAP1; NbExp=3; IntAct=EBI-347658, EBI-11110431;
CC Q9UHI6; P57678: GEMIN4; NbExp=7; IntAct=EBI-347658, EBI-356700;
CC Q9UHI6; P42858: HTT; NbExp=6; IntAct=EBI-347658, EBI-466029;
CC Q9UHI6; P51608: MECP2; NbExp=3; IntAct=EBI-347658, EBI-1189067;
CC Q9UHI6; Q16637: SMN2; NbExp=10; IntAct=EBI-347658, EBI-395421;
CC Q9UHI6; O14656-2: TOR1A; NbExp=3; IntAct=EBI-347658, EBI-25847109;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10601333,
CC ECO:0000305|PubMed:12095920}. Nucleus, gem
CC {ECO:0000269|PubMed:10601333, ECO:0000305|PubMed:10383418}.
CC Note=Localized in subnuclear structures next to coiled bodies, called
CC Gemini of Cajal bodies (Gems). {ECO:0000269|PubMed:10601333}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UHI6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UHI6-2; Sequence=VSP_056505, VSP_056506;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX20 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF171063; AAF14544.1; -; mRNA.
DR EMBL; AF106019; AAD42744.1; -; mRNA.
DR EMBL; AK001506; BAA91727.1; -; mRNA.
DR EMBL; AK301697; BAG63169.1; -; mRNA.
DR EMBL; AL049557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011556; AAH11556.1; -; mRNA.
DR EMBL; AL133598; CAB63734.2; -; mRNA.
DR CCDS; CCDS842.1; -. [Q9UHI6-1]
DR PIR; T43476; T43476.
DR RefSeq; NP_009135.4; NM_007204.4. [Q9UHI6-1]
DR PDB; 2OXC; X-ray; 1.30 A; A/B=41-268.
DR PDB; 3B7G; X-ray; 1.90 A; A/B=41-268.
DR PDBsum; 2OXC; -.
DR PDBsum; 3B7G; -.
DR AlphaFoldDB; Q9UHI6; -.
DR SMR; Q9UHI6; -.
DR BioGRID; 116387; 188.
DR ComplexPortal; CPX-6031; SMN complex.
DR CORUM; Q9UHI6; -.
DR DIP; DIP-32606N; -.
DR IntAct; Q9UHI6; 79.
DR MINT; Q9UHI6; -.
DR STRING; 9606.ENSP00000358716; -.
DR GlyGen; Q9UHI6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UHI6; -.
DR PhosphoSitePlus; Q9UHI6; -.
DR BioMuta; DDX20; -.
DR DMDM; 12643886; -.
DR EPD; Q9UHI6; -.
DR jPOST; Q9UHI6; -.
DR MassIVE; Q9UHI6; -.
DR MaxQB; Q9UHI6; -.
DR PaxDb; Q9UHI6; -.
DR PeptideAtlas; Q9UHI6; -.
DR PRIDE; Q9UHI6; -.
DR ProteomicsDB; 5385; -.
DR ProteomicsDB; 84357; -. [Q9UHI6-1]
DR Antibodypedia; 1125; 358 antibodies from 36 providers.
DR DNASU; 11218; -.
DR Ensembl; ENST00000369702.5; ENSP00000358716.4; ENSG00000064703.13. [Q9UHI6-1]
DR Ensembl; ENST00000533164.6; ENSP00000434085.1; ENSG00000064703.13. [Q9UHI6-2]
DR Ensembl; ENST00000679724.1; ENSP00000505857.1; ENSG00000064703.13. [Q9UHI6-1]
DR GeneID; 11218; -.
DR KEGG; hsa:11218; -.
DR MANE-Select; ENST00000369702.5; ENSP00000358716.4; NM_007204.5; NP_009135.4.
DR UCSC; uc001ebs.4; human. [Q9UHI6-1]
DR CTD; 11218; -.
DR DisGeNET; 11218; -.
DR GeneCards; DDX20; -.
DR HGNC; HGNC:2743; DDX20.
DR HPA; ENSG00000064703; Tissue enriched (testis).
DR MIM; 606168; gene.
DR neXtProt; NX_Q9UHI6; -.
DR OpenTargets; ENSG00000064703; -.
DR PharmGKB; PA27209; -.
DR VEuPathDB; HostDB:ENSG00000064703; -.
DR eggNOG; KOG4284; Eukaryota.
DR GeneTree; ENSGT00940000158400; -.
DR HOGENOM; CLU_1854485_0_0_1; -.
DR InParanoid; Q9UHI6; -.
DR OMA; ECISGSM; -.
DR PhylomeDB; Q9UHI6; -.
DR TreeFam; TF352222; -.
DR PathwayCommons; Q9UHI6; -.
DR Reactome; R-HSA-191859; snRNP Assembly.
DR Reactome; R-HSA-9754678; SARS-CoV-2 modulates host translation machinery.
DR SignaLink; Q9UHI6; -.
DR SIGNOR; Q9UHI6; -.
DR BioGRID-ORCS; 11218; 726 hits in 1048 CRISPR screens.
DR ChiTaRS; DDX20; human.
DR EvolutionaryTrace; Q9UHI6; -.
DR GeneWiki; DDX20; -.
DR GenomeRNAi; 11218; -.
DR Pharos; Q9UHI6; Tbio.
DR PRO; PR:Q9UHI6; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UHI6; protein.
DR Bgee; ENSG00000064703; Expressed in sperm and 172 other tissues.
DR Genevisible; Q9UHI6; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0097504; C:Gemini of coiled bodies; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IEA:Ensembl.
DR GO; GO:0032797; C:SMN complex; IDA:UniProtKB.
DR GO; GO:0034719; C:SMN-Sm protein complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0048477; P:oogenesis; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IGI:MGI.
DR GO; GO:0050810; P:regulation of steroid biosynthetic process; IEA:Ensembl.
DR GO; GO:0006396; P:RNA processing; TAS:ProtInc.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB.
DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; TAS:ProtInc.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cytoplasm; DNA-binding;
KW Helicase; Hydrolase; mRNA processing; mRNA splicing; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..824
FT /note="Probable ATP-dependent RNA helicase DDX20"
FT /id="PRO_0000055025"
FT DOMAIN 93..264
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 299..448
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 456..548
FT /note="SMN interacting"
FT REGION 488..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 62..90
FT /note="Q motif"
FT MOTIF 211..214
FT /note="DEAD box"
FT COMPBIAS 489..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 109..114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 552
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 654
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 656
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 688
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243"
FT MOD_RES 703
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 705
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 133..138
FT /note="ILILAP -> AELSNS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056505"
FT VAR_SEQ 139..824
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056506"
FT VARIANT 636
FT /note="I -> T (in dbSNP:rs197412)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_057231"
FT VARIANT 693
FT /note="R -> S (in dbSNP:rs197414)"
FT /id="VAR_057232"
FT VARIANT 762
FT /note="I -> T (in dbSNP:rs85276)"
FT /id="VAR_057233"
FT CONFLICT 5
FT /note="F -> V (in Ref. 2; AAD42744)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="Y -> C (in Ref. 3; BAA91727)"
FT /evidence="ECO:0000305"
FT CONFLICT 639
FT /note="R -> K (in Ref. 1; AAF14544)"
FT /evidence="ECO:0000305"
FT CONFLICT 659
FT /note="Y -> H (in Ref. 2; AAD42744)"
FT /evidence="ECO:0000305"
FT CONFLICT 676
FT /note="G -> S (in Ref. 1; AAF14544)"
FT /evidence="ECO:0000305"
FT CONFLICT 703
FT /note="S -> T (in Ref. 1; AAF14544)"
FT /evidence="ECO:0000305"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:2OXC"
FT HELIX 71..79
FT /evidence="ECO:0007829|PDB:2OXC"
FT HELIX 87..97
FT /evidence="ECO:0007829|PDB:2OXC"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:2OXC"
FT HELIX 112..123
FT /evidence="ECO:0007829|PDB:2OXC"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:2OXC"
FT HELIX 140..153
FT /evidence="ECO:0007829|PDB:2OXC"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:2OXC"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:2OXC"
FT HELIX 171..177
FT /evidence="ECO:0007829|PDB:2OXC"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:2OXC"
FT HELIX 188..196
FT /evidence="ECO:0007829|PDB:2OXC"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:2OXC"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:2OXC"
FT HELIX 213..217
FT /evidence="ECO:0007829|PDB:2OXC"
FT HELIX 223..232
FT /evidence="ECO:0007829|PDB:2OXC"
FT STRAND 238..244
FT /evidence="ECO:0007829|PDB:2OXC"
FT HELIX 248..254
FT /evidence="ECO:0007829|PDB:2OXC"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:2OXC"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:2OXC"
SQ SEQUENCE 824 AA; 92241 MW; 76712F014B2A0CF2 CRC64;
MAAAFEASGA LAAVATAMPA EHVAVQVPAP EPTPGPVRIL RTAQDLSSPR TRTGDVLLAE
PADFESLLLS RPVLEGLRAA GFERPSPVQL KAIPLGRCGL DLIVQAKSGT GKTCVFSTIA
LDSLVLENLS TQILILAPTR EIAVQIHSVI TAIGIKMEGL ECHVFIGGTP LSQDKTRLKK
CHIAVGSPGR IKQLIELDYL NPGSIRLFIL DEADKLLEEG SFQEQINWIY SSLPASKQML
AVSATYPEFL ANALTKYMRD PTFVRLNSSD PSLIGLKQYY KVVNSYPLAH KVFEEKTQHL
QELFSRIPFN QALVFSNLHS RAQHLADILS SKGFPAECIS GNMNQNQRLD AMAKLKHFHC
RVLISTDLTS RGIDAEKVNL VVNLDVPLDW ETYMHRIGRA GRFGTLGLTV TYCCRGEEEN
MMMRIAQKCN INLLPLPDPI PSGLMEECVD WDVEVKAAVH TYGIASVPNQ PLKKQIQKIE
RTLQIQKAHG DHMASSRNNS VSGLSVKSKN NTKQKLPVKS HSECGIIEKA TSPKELGCDR
QSEEQMKNSV QTPVENSTNS QHQVKEALPV SLPQIPCLSS FKIHQPYTLT FAELVEDYEH
YIKEGLEKPV EIIRHYTGPG DQTVNPQNGF VRNKVIEQRV PVLASSSQSG DSESDSDSYS
SRTSSQSKGN KSYLEGSSDN QLKDSESTPV DDRISLEQPP NGSDTPNPEK YQESPGIQMK
TRLKEGASQR AKQSRRNLPR RSSFRLQTEA QEDDWYDCHR EIRLSFSDTY QDYEEYWRAY
YRAWQEYYAA ASHSYYWNAQ RHPSWMAAYH MNTIYLQEMM HSNQ
